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AlphaFold monomer V2.0 prediction for segregation and condensation protein a (Q98R95)

Analyse AlphaFold monomer V2.0 prediction for segregation and condensation protein a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q98R95
Type
protein
Length
249 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
Molecule
Segregation and condensation protein a
UniProt
Q98R95
Pockets
3 · best druggability 0.51

Structure

1 distinct chain · 57% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASegregation and condensation protein aprotein24957% helix, 5% strandQ98R95

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12370.510.7529empty
2930.430.7824empty
3530.270.7412empty

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